Q86W56 (PARG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poly(ADP-ribose) glycohydrolase
EC=3.2.1.143

Gene names

Name:

PARG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	976 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. PARG acts both as an endo- and exoglycosidase, releasing PAR of different length as well as ADP-ribose monomers. Required for retinoid acid-dependent gene transactivation, probably by dePARsylating histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Ref.17
Catalytic activity	Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose. Ref.5
Subunit structure	Interacts with PCNA. Ref.15
Subcellular location	Isoform 1: Nucleus. Note: Co-localizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage. Ref.4 Ref.5 Ref.8 Ref.15 Isoform 2: Cytoplasm Ref.4 Ref.5 Ref.8 Ref.15. Note: Translocates to the nucleus in response to DNA damage. Ref.4 Ref.5 Ref.8 Ref.15 Isoform 3: Cytoplasm Ref.4 Ref.5 Ref.8 Ref.15. Isoform 4: Cytoplasm Ref.4 Ref.5 Ref.8 Ref.15. Mitochondrion Ref.4 Ref.5 Ref.8 Ref.15. Isoform 5: Mitochondrion matrix Ref.4 Ref.5 Ref.8 Ref.15.
Tissue specificity	Ubiquitously expressed. Ref.1
Domain	The PIP-box mediates interaction with PCNA and localization to replication foci.
Sequence similarities	Belongs to the poly(ADP-ribose) glycohydrolase family.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro detection of bacterium Inferred from electronic annotation. Source: Compara response to DNA damage stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Traceable author statement PubMed 9925755. Source: ProtInc cytosol Inferred from electronic annotation. Source: Compara mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular_function	poly(ADP-ribose) glycohydrolase activity Inferred from direct assay PubMed 15450800. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86W56-1)

Also known as: hPARG111;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q86W56-2)

Also known as: hPARG102;

The sequence of this isoform differs from the canonical sequence as follows:
     1-82: Missing.

Isoform 3 (identifier: Q86W56-3)

Also known as: hPARG99;

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.

Isoform 4 (identifier: Q86W56-4)

Also known as: hPARG60;

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MNAGPGCEPCTKRPR → MVQAGAEKDAQSISL
     16-423: Missing.
     485-526: RVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDE → W

Note: Catalytically inactive.

Isoform 5 (identifier: Q86W56-5)

Also known as: hPARG55;

The sequence of this isoform differs from the canonical sequence as follows:
     1-460: Missing.
     485-526: RVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDE → W

Note: Catalytically inactive.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 976

976

Poly(ADP-ribose) glycohydrolase

PRO_0000066602

Regions

Region

1 – 456

456

A-domain

Region

610 – 795

186

Catalytic

Region

726 – 727

2

Substrate binding By similarity

Region

869 – 874

6

Substrate binding By similarity

Motif

10 – 16

7

Nuclear localization signal Ref.2

Motif

76 – 83

8

PIP-box (PCNA interacting peptide)

Sites

Active site

737

1

By similarity

Active site

755

1

By similarity

Active site

756

1

By similarity

Binding site

740

1

Substrate By similarity

Binding site

754

1

Substrate; via amide nitrogen By similarity

Binding site

795

1

Substrate By similarity

Amino acid modifications

Modified residue

133

1

Phosphoserine Ref.10

Modified residue

137

1

Phosphoserine Ref.10

Modified residue

197

1

Phosphoserine Ref.10 Ref.11 Ref.12

Modified residue

199

1

Phosphothreonine Ref.10 Ref.11 Ref.12

Modified residue

261

1

Phosphoserine By similarity

Modified residue

264

1

Phosphoserine By similarity

Modified residue

298

1

Phosphoserine Ref.11

Modified residue

302

1

Phosphoserine Ref.16

Natural variations

Alternative sequence

1 – 460

460

Missing in isoform 5.

VSP_044674

Alternative sequence

1 – 108

108

Missing in isoform 3.

VSP_011770

Alternative sequence

1 – 82

82

Missing in isoform 2.

VSP_011769

Alternative sequence

1 – 15

15

MNAGP…TKRPR → MVQAGAEKDAQSISL in isoform 4.

VSP_044675

Alternative sequence

16 – 423

408

Missing in isoform 4.

VSP_044676

Alternative sequence

485 – 526

42

RVDLL…PVEDE → W in isoform 4 and isoform 5.

VSP_044677

Experimental info

Mutagenesis

12

1

K → A: Abolishes nuclear targeting; when associated with G-13. Ref.2

Mutagenesis

13

1

R → G: Abolishes nuclear targeting; when associated with A-12. Ref.2

Mutagenesis

36

1

R → A: No effect. Ref.2

Mutagenesis

37

1

R → G: No effect. Ref.2

Sequence conflict

13 – 14

2

RP → AT in AAB61614. Ref.3

Sequence conflict

61

1

R → Q in AAB61614. Ref.3

Sequence conflict

127

1

E → V in AAB61614. Ref.3

Sequence conflict

138

1

P → L in AAB61614. Ref.3

Sequence conflict

227

1

Q → H in AAB61614. Ref.3

Sequence conflict

242

1

D → H in AAB61614. Ref.3

Sequence conflict

260

1

E → K in AAB61614. Ref.3

Sequence conflict

275

1

P → S in AAB61614. Ref.3

Sequence conflict

282

1

T → I in AAB61614. Ref.3

Sequence conflict

414

1

F → L in AAB61614. Ref.3

Sequence conflict

466

1

R → Q in AFM56043. Ref.5

Sequence conflict

484

1

I → V in AFM56043. Ref.5

Sequence conflict

814 – 815

2

WQ → CE in AAB61614. Ref.3

Sequence conflict

817

1

R → H in AAH52966. Ref.7

Secondary structure

1

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976

Helix Strand Turn

Details...

Beta strand

452 – 456

5

Helix

458 – 460

3

Turn

464 – 467

4

Beta strand

480 – 482

3

Helix

486 – 488

3

Beta strand

497 – 501

5

Beta strand

520 – 522

3

Beta strand

532 – 534

3

Helix

535 – 543

9

Helix

550 – 559

10

Helix

562 – 564

3

Turn

565 – 567

3

Helix

571 – 579

9

Helix

583 – 591

9

Helix

593 – 602

10

Helix

604 – 607

4

Beta strand

621 – 626

6

Helix

627 – 638

12

Turn

652 – 655

4

Helix

662 – 665

4

Helix

672 – 688

17

Beta strand

694 – 701

8

Helix

708 – 710

3

Beta strand

718 – 724

7

Helix

726 – 729

4

Turn

730 – 732

3

Beta strand

733 – 739

7

Turn

743 – 750

8

Helix

754 – 761

8

Helix

763 – 767

5

Helix

768 – 771

4

Beta strand

779 – 784

6

Beta strand

790 – 793

4

Helix

796 – 798

3

Beta strand

800 – 804

5

Beta strand

815 – 818

4

Beta strand

820 – 825

6

Helix

832 – 836

5

Helix

838 – 852

15

Helix

859 – 861

3

Beta strand

865 – 868

4

Helix

873 – 875

3

Helix

879 – 892

14

Beta strand

897 – 900

4

Helix

905 – 920

16

Helix

925 – 939

15

Turn

940 – 942

3

Beta strand

945 – 947

3

Helix

952 – 961

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (hPARG111) [UniParc]. Last modified June 1, 2003. Version 1. Checksum: D6646353C6D0180E	FASTA	976	111,110
	10 20 30 40 50 60 MNAGPGCEPC TKRPRWGAAT TSPAASDARS FPSRQRRVLD PKDAHVQFRV PPSSPACVPG 70 80 90 100 110 120 RAGQHRGSAT SLVFKQKTIT SWMDTKGIKT AESESLDSKE NNNTRIESMM SSVQKDNFYQ 130 140 150 160 170 180 HNVEKLENVS QLSLDKSPTE KSTQYLNQHQ TAAMCKWQNE GKHTEQLLES EPQTVTLVPE 190 200 210 220 230 240 QFSNANIDRS PQNDDHSDTD SEENRDNQQF LTTVKLANAK QTTEDEQARE AKSHQKCSKS 250 260 270 280 290 300 CDPGEDCASC QQDEIDVVPE SPLSDVGSED VGTGPKNDNK LTRQESCLGN SPPFEKESEP 310 320 330 340 350 360 ESPMDVDNSK NSCQDSEADE ETSPGFDEQE DGSSSQTANK PSRFQARDAD IEFRKRYSTK 370 380 390 400 410 420 GGEVRLHFQF EGGESRTGMN DLNAKLPGNI SSLNVECRNS KQHGKKDSKI TDHFMRLPKA 430 440 450 460 470 480 EDRRKEQWET KHQRTERKIP KYVPPHLSPD KKWLGTPIEE MRRMPRCGIR LPLLRPSANH 490 500 510 520 530 540 TVTIRVDLLR AGEVPKPFPT HYKDLWDNKH VKMPCSEQNL YPVEDENGER TAGSRWELIQ 550 560 570 580 590 600 TALLNKFTRP QNLKDAILKY NVAYSKKWDF TALIDFWDKV LEEAEAQHLY QSILPDMVKI 610 620 630 640 650 660 ALCLPNICTQ PIPLLKQKMN HSITMSQEQI ASLLANAFFC TFPRRNAKMK SEYSSYPDIN 670 680 690 700 710 720 FNRLFEGRSS RKPEKLKTLF CYFRRVTEKK PTGLVTFTRQ SLEDFPEWER CEKPLTRLHV 730 740 750 760 770 780 TYEGTIEENG QGMLQVDFAN RFVGGGVTSA GLVQEEIRFL INPELIISRL FTEVLDHNEC 790 800 810 820 830 840 LIITGTEQYS EYTGYAETYR WSRSHEDGSE RDDWQRRCTE IVAIDALHFR RYLDQFVPEK 850 860 870 880 890 900 MRRELNKAYC GFLRPGVSSE NLSAVATGNW GCGAFGGDAR LKALIQILAA AAAERDVVYF 910 920 930 940 950 960 TFGDSELMRD IYSMHIFLTE RKLTVGDVYK LLLRYYNEEC RNCSTPGPDI KLYPFIYHAV 970 ESCAETADHS GQRTGT
	Isoform 2 (hPARG102) [UniParc]. Checksum: 666B77E891E4A500	FASTA	894	102,312
	10 20 30 40 50 60 MDTKGIKTAE SESLDSKENN NTRIESMMSS VQKDNFYQHN VEKLENVSQL SLDKSPTEKS 70 80 90 100 110 120 TQYLNQHQTA AMCKWQNEGK HTEQLLESEP QTVTLVPEQF SNANIDRSPQ NDDHSDTDSE 130 140 150 160 170 180 ENRDNQQFLT TVKLANAKQT TEDEQAREAK SHQKCSKSCD PGEDCASCQQ DEIDVVPESP 190 200 210 220 230 240 LSDVGSEDVG TGPKNDNKLT RQESCLGNSP PFEKESEPES PMDVDNSKNS CQDSEADEET 250 260 270 280 290 300 SPGFDEQEDG SSSQTANKPS RFQARDADIE FRKRYSTKGG EVRLHFQFEG GESRTGMNDL 310 320 330 340 350 360 NAKLPGNISS LNVECRNSKQ HGKKDSKITD HFMRLPKAED RRKEQWETKH QRTERKIPKY 370 380 390 400 410 420 VPPHLSPDKK WLGTPIEEMR RMPRCGIRLP LLRPSANHTV TIRVDLLRAG EVPKPFPTHY 430 440 450 460 470 480 KDLWDNKHVK MPCSEQNLYP VEDENGERTA GSRWELIQTA LLNKFTRPQN LKDAILKYNV 490 500 510 520 530 540 AYSKKWDFTA LIDFWDKVLE EAEAQHLYQS ILPDMVKIAL CLPNICTQPI PLLKQKMNHS 550 560 570 580 590 600 ITMSQEQIAS LLANAFFCTF PRRNAKMKSE YSSYPDINFN RLFEGRSSRK PEKLKTLFCY 610 620 630 640 650 660 FRRVTEKKPT GLVTFTRQSL EDFPEWERCE KPLTRLHVTY EGTIEENGQG MLQVDFANRF 670 680 690 700 710 720 VGGGVTSAGL VQEEIRFLIN PELIISRLFT EVLDHNECLI ITGTEQYSEY TGYAETYRWS 730 740 750 760 770 780 RSHEDGSERD DWQRRCTEIV AIDALHFRRY LDQFVPEKMR RELNKAYCGF LRPGVSSENL 790 800 810 820 830 840 SAVATGNWGC GAFGGDARLK ALIQILAAAA AERDVVYFTF GDSELMRDIY SMHIFLTERK 850 860 870 880 890 LTVGDVYKLL LRYYNEECRN CSTPGPDIKL YPFIYHAVES CAETADHSGQ RTGT
	Isoform 3 (hPARG99) [UniParc]. Checksum: 85BCE7201ABABA5F	FASTA	868	99,432
	10 20 30 40 50 60 MMSSVQKDNF YQHNVEKLEN VSQLSLDKSP TEKSTQYLNQ HQTAAMCKWQ NEGKHTEQLL 70 80 90 100 110 120 ESEPQTVTLV PEQFSNANID RSPQNDDHSD TDSEENRDNQ QFLTTVKLAN AKQTTEDEQA 130 140 150 160 170 180 REAKSHQKCS KSCDPGEDCA SCQQDEIDVV PESPLSDVGS EDVGTGPKND NKLTRQESCL 190 200 210 220 230 240 GNSPPFEKES EPESPMDVDN SKNSCQDSEA DEETSPGFDE QEDGSSSQTA NKPSRFQARD 250 260 270 280 290 300 ADIEFRKRYS TKGGEVRLHF QFEGGESRTG MNDLNAKLPG NISSLNVECR NSKQHGKKDS 310 320 330 340 350 360 KITDHFMRLP KAEDRRKEQW ETKHQRTERK IPKYVPPHLS PDKKWLGTPI EEMRRMPRCG 370 380 390 400 410 420 IRLPLLRPSA NHTVTIRVDL LRAGEVPKPF PTHYKDLWDN KHVKMPCSEQ NLYPVEDENG 430 440 450 460 470 480 ERTAGSRWEL IQTALLNKFT RPQNLKDAIL KYNVAYSKKW DFTALIDFWD KVLEEAEAQH 490 500 510 520 530 540 LYQSILPDMV KIALCLPNIC TQPIPLLKQK MNHSITMSQE QIASLLANAF FCTFPRRNAK 550 560 570 580 590 600 MKSEYSSYPD INFNRLFEGR SSRKPEKLKT LFCYFRRVTE KKPTGLVTFT RQSLEDFPEW 610 620 630 640 650 660 ERCEKPLTRL HVTYEGTIEE NGQGMLQVDF ANRFVGGGVT SAGLVQEEIR FLINPELIIS 670 680 690 700 710 720 RLFTEVLDHN ECLIITGTEQ YSEYTGYAET YRWSRSHEDG SERDDWQRRC TEIVAIDALH 730 740 750 760 770 780 FRRYLDQFVP EKMRRELNKA YCGFLRPGVS SENLSAVATG NWGCGAFGGD ARLKALIQIL 790 800 810 820 830 840 AAAAAERDVV YFTFGDSELM RDIYSMHIFL TERKLTVGDV YKLLLRYYNE ECRNCSTPGP 850 860 DIKLYPFIYH AVESCAETAD HSGQRTGT
	Isoform 4 (hPARG60) [UniParc]. Checksum: 0FBB26152C56D33D	FASTA	527	60,873
	10 20 30 40 50 60 MVQAGAEKDA QSISLRKEQW ETKHQRTERK IPKYVPPHLS PDKKWLGTPI EEMRRMPRCG 70 80 90 100 110 120 IRLPLLRPSA NHTVTIWNGE RTAGSRWELI QTALLNKFTR PQNLKDAILK YNVAYSKKWD 130 140 150 160 170 180 FTALIDFWDK VLEEAEAQHL YQSILPDMVK IALCLPNICT QPIPLLKQKM NHSITMSQEQ 190 200 210 220 230 240 IASLLANAFF CTFPRRNAKM KSEYSSYPDI NFNRLFEGRS SRKPEKLKTL FCYFRRVTEK 250 260 270 280 290 300 KPTGLVTFTR QSLEDFPEWE RCEKPLTRLH VTYEGTIEEN GQGMLQVDFA NRFVGGGVTS 310 320 330 340 350 360 AGLVQEEIRF LINPELIISR LFTEVLDHNE CLIITGTEQY SEYTGYAETY RWSRSHEDGS 370 380 390 400 410 420 ERDDWQRRCT EIVAIDALHF RRYLDQFVPE KMRRELNKAY CGFLRPGVSS ENLSAVATGN 430 440 450 460 470 480 WGCGAFGGDA RLKALIQILA AAAAERDVVY FTFGDSELMR DIYSMHIFLT ERKLTVGDVY 490 500 510 520 KLLLRYYNEE CRNCSTPGPD IKLYPFIYHA VESCAETADH SGQRTGT
	Isoform 5 (hPARG55) [UniParc]. Checksum: 5443EFFA21AA84CE	FASTA	475	54,794
	10 20 30 40 50 60 MRRMPRCGIR LPLLRPSANH TVTIWNGERT AGSRWELIQT ALLNKFTRPQ NLKDAILKYN 70 80 90 100 110 120 VAYSKKWDFT ALIDFWDKVL EEAEAQHLYQ SILPDMVKIA LCLPNICTQP IPLLKQKMNH 130 140 150 160 170 180 SITMSQEQIA SLLANAFFCT FPRRNAKMKS EYSSYPDINF NRLFEGRSSR KPEKLKTLFC 190 200 210 220 230 240 YFRRVTEKKP TGLVTFTRQS LEDFPEWERC EKPLTRLHVT YEGTIEENGQ GMLQVDFANR 250 260 270 280 290 300 FVGGGVTSAG LVQEEIRFLI NPELIISRLF TEVLDHNECL IITGTEQYSE YTGYAETYRW 310 320 330 340 350 360 SRSHEDGSER DDWQRRCTEI VAIDALHFRR YLDQFVPEKM RRELNKAYCG FLRPGVSSEN 370 380 390 400 410 420 LSAVATGNWG CGAFGGDARL KALIQILAAA AAERDVVYFT FGDSELMRDI YSMHIFLTER 430 440 450 460 470 KLTVGDVYKL LLRYYNEECR NCSTPGPDIK LYPFIYHAVE SCAETADHSG QRTGT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common promoter sequence it shares with inner mitochondrial membrane translocase 23 (TIM23)." Meyer R.G., Meyer-Ficca M.L., Jacobson E.L., Jacobson M.K. Gene 314:181-190(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Skin.
[2]	"Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments." Meyer-Ficca M.L., Meyer R.G., Coyle D.L., Jacobson E.L., Jacobson M.K. Exp. Cell Res. 297:521-532(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), MUTAGENESIS OF LYS-12; ARG-13; ARG-36 AND ARG-37, NUCLEAR LOCALIZATION SIGNAL. Tissue: Skin.
[3]	"Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization." Ame J.-C., Apiou F., Jacobson E.L., Jacobson M.K. Cytogenet. Cell Genet. 85:269-270(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-ribose) glycohydrolase (PARG) activity." Meyer R.G., Meyer-Ficca M.L., Whatcott C.J., Jacobson E.L., Jacobson M.K. Exp. Cell Res. 313:2920-2936(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION. Tissue: Testis.
[5]	"ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose)." Niere M., Mashimo M., Agledal L., Dolle C., Kasamatsu A., Kato J., Moss J., Ziegler M. J. Biol. Chem. 287:16088-16102(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPICING (ISOFORMS 4 AND 5), ABSENCE OF CATALYTIC ACTIVITY (ISOFORMS 4 AND 5), SUBCELLULAR LOCATION. Tissue: Peripheral blood monocyte.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Brain cortex, Hippocampus and Testis.
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin and Testis.
[8]	"Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage." Haince J.F., Ouellet M.E., McDonald D., Hendzel M.J., Poirier G.G. Biochim. Biophys. Acta 1763:226-237(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).
[9]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-137; SER-197 AND THR-199, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Proteomic investigation of phosphorylation sites in poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase." Gagne J.P., Moreel X., Gagne P., Labelle Y., Droit A., Chevalier-Pare M., Bourassa S., McDonald D., Hendzel M.J., Prigent C., Poirier G.G. J. Proteome Res. 8:1014-1029(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-197; THR-199 AND SER-298.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND THR-199, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNA-dependent mechanisms." Mortusewicz O., Fouquerel E., Ame J.C., Leonhardt H., Schreiber V. Nucleic Acids Res. 39:5045-5056(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION (ISOFORM 1), INTERACTION WITH PCNA.
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, MASS SPECTROMETRY.
[17]	"Poly (ADP-ribose) glycohydrolase regulates retinoic acid receptor-mediated gene expression." Le May N., Iltis I., Ame J.C., Zhovmer A., Biard D., Egly J.M., Schreiber V., Coin F. Mol. Cell 48:785-798(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY258587 mRNA. Translation: AAP83314.1.
AY575848 mRNA. Translation: AAT66421.1.
AY575849 mRNA. Translation: AAT66422.1.
AF005043 mRNA. Translation: AAB61614.1.
EF382674 mRNA. Translation: ABR10027.1.
JQ890226 mRNA. Translation: AFM56043.1.
AK295786 mRNA. Translation: BAG58607.1.
AK302560 mRNA. Translation: BAG63826.1.
AK314909 mRNA. Translation: BAG37421.1.
BC050560 mRNA. Translation: AAH50560.1.
BC052966 mRNA. Translation: AAH52966.1.

IPI

IPI00470744.
IPI00759749.
IPI00787604.

RefSeq

NP_003622.2. NM_003631.2.

UniGene

Hs.10136.
Hs.535298.
Hs.732225.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4A0D	X-ray	1.75	A	448-976	[»]
4B1G	X-ray	1.83	A	448-976	[»]
4B1H	X-ray	2.00	A	448-976	[»]
4B1I	X-ray	2.14	A	448-976	[»]
4B1J	X-ray	2.08	A	448-976	[»]

ProteinModelPortal

Q86W56.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000384408.

PTM databases

PhosphoSite

Q86W56.

Polymorphism databases

DMDM

56417893.

Proteomic databases

PaxDb

Q86W56.

PRIDE

Q86W56.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000402038; ENSP00000384408; ENSG00000227345.

GeneID

8505.

KEGG

hsa:8505.

UCSC

uc001jif.3. human.
uc010qgx.2. human.

Organism-specific databases

CTD

8505.

GeneCards

GC10M051026.

H-InvDB

HIX0127080.

HGNC

HGNC:8605. PARG.

HPA

HPA021819.

MIM

603501. gene.

neXtProt

NX_Q86W56.

PharmGKB

PA32940.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG254589.

HOVERGEN

HBG053510.

InParanoid

Q86W56.

KO

K07759.

Gene expression databases

ArrayExpress

Q86W56.

Bgee

Q86W56.

CleanEx

HS_PARG.

Genevestigator

Q86W56.

GermOnline

ENSG00000204155. Homo sapiens.

Family and domain databases

InterPro

IPR007724. Poly_GlycHdrlase.
[Graphical view]

PANTHER

PTHR12837. PTHR12837. 1 hit.

Pfam

PF05028. PARG_cat. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q86W56.

ChEMBL

CHEMBL1795143.

ChiTaRS

PARG. human.

GenomeRNAi

8505.

NextBio

31829.

PMAP-CutDB

Q86W56.

SOURCE

Search...

Entry information

Entry name

PARG_HUMAN

Accession

Primary (citable) accession number: Q86W56
Secondary accession number(s): A5YBK3 , B2RC24, B4DIU5, B4DYR4, I6RUV3, Q6E4P6, Q6E4P7, Q7Z742, Q9Y4W7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2004
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.